3ZZ5
Crystal structure of 3C protease of coxsackievirus B3 complexed with alpha, beta-unsaturated ethyl ester inhibitor 74
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MARMOSAIC 225 mm CCD |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 76.880, 63.960, 39.550 |
| Unit cell angles | 90.00, 115.95, 90.00 |
Refinement procedure
| Resolution | 46.950 - 2.200 |
| R-factor | 0.21566 |
| Rwork | 0.212 |
| R-free | 0.30626 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | CRYSTAL STRUCTURE OF COXSACKIEVIURS B3 3C PROTEASE |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.823 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0110) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 35.560 | 2.320 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.060 | 0.470 |
| Number of reflections | 8045 | |
| <I/σ(I)> | 9 | 2.3 |
| Completeness [%] | 91.7 | 91.5 |
| Redundancy | 2.6 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 100 MM TRIS-HCL PH 8.5, 0.2 M MAGNESIUM CHLORIDE, AND 22% PEG 4000; SITTING DROP |
